Daniel T. Hansen

Multipartite Fluorogenic Sensors for Monitoring Tyrosine Phosphatase Activity

Daniel T. Hansen, Julian Tu, Alison W. Bouck, Cheryl L. Mathis et autres

Abstract Fluorogenic substrates are essential tools for studying the activity of many enzymes including the protein tyrosine phosphatases (PTPs). Here, we have taken the first step toward the development of genetically encodable sensors for PTP activity using fluorescent and fluorogen‐activating proteins. The …

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The mechanism of covalent inhibition of LAR phosphatase by illudalic acid

Daniel T. Hansen, Nicole J. Rueb, Nathan D. Levinzon, Thomas E. Cheatham et autres

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Structure of the Cdc48 segregase in the act of unfolding an authentic substrate

Ian Cooney, Han Han, Michael G. Stewart, Richard H. Carson et autres

Protein unfolding, one substrate at a time Ubiquitin marks proteins for degradation by the proteasome. However, many substrates cannot be directly degraded because they are well folded or are located in cell membranes or in multimeric complexes. These proteins are first unfolded …

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Cdc48 Hexamer in a complex with substrate and Shp1(Ubx Domain)

Ian Cooney, Hyunsoo Han, Michael G. Stewart, Richard H. Carson et autres

Cdc48 Hexamer (Subunits A to E) with substrate bound to the central pore

Ian Cooney, Heping Han, Michael G. Stewart, Richard H. Carson et autres